ID   TRMYL_ALCBS             Reviewed;         200 AA.
AC   Q0VNR6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Putative pseudouridine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00587};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00587};
GN   OrderedLocusNames=ABO_1734;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.
CC       {ECO:0000255|HAMAP-Rule:MF_00587}.
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DR   EMBL; AM286690; CAL17182.1; -; Genomic_DNA.
DR   RefSeq; WP_011589015.1; NC_008260.1.
DR   AlphaFoldDB; Q0VNR6; -.
DR   SMR; Q0VNR6; -.
DR   STRING; 393595.ABO_1734; -.
DR   EnsemblBacteria; CAL17182; CAL17182; ABO_1734.
DR   KEGG; abo:ABO_1734; -.
DR   eggNOG; COG1901; Bacteria.
DR   HOGENOM; CLU_107018_0_0_6; -.
DR   OMA; HADHCII; -.
DR   OrthoDB; 1311630at2; -.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:InterPro.
DR   CDD; cd18087; TrmY-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00587; tRNA_methyltr_TrmY; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR007158; TrmY.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR40703; PTHR40703; 1.
DR   Pfam; PF04013; Methyltrn_RNA_2; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..200
FT                   /note="Putative pseudouridine methyltransferase"
FT                   /id="PRO_1000025462"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         187
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ   SEQUENCE   200 AA;  22085 MW;  2A14E5791972CA4C CRC64;
     MRTFVLRARA ASTHSQTLLA NVGGDAHSEI LAHTLMNAIF VAQSHRDDVV VHLVLESTQD
     YSRTITFVAA EMRDIGGFHE QALLAKVVRA LDASAGMGKE QMKAVESGIT VRTQSFEKVV
     KELAEDGHQL YMMDPKGENI RELDFAQKPC FLLTDHIPMP KKSFNSLKRL GTEKISLGPT
     MLFASQCVVL INNELDLAGF